Bacterial infections and immunology

Identifying new methods to diagnose, prevent and treat infections before they become life-threatening

 

Professor Henderson's research group studies bacteria and their interaction with humans and animals.

Their research is focused on the discovery of genes that are important for building the cell membrane of bacteria. Using genetic, biochemical and structural techniques they study the activity, regulation and function of these genes and their products. Using mice as a model they assess if the products of these genes are important for infectious disease.

The group's purpose is to apply this understanding to the diagnosis, prevention and treatment of infections that can lead to life-threatening disease in humans and animals. Professor Henderson seeks targets for developing new antibiotics, vaccines and novel therapies.

 

Group leader

Professor Ian Henderson

Professor Ian Henderson

Group Leader, Bacterial infections and immunology

Director, Institute for Molecular Bioscience

  +61 7 334 62110
  i.henderson@imb.uq.edu.au
  UQ Researcher Profile

Aims to achieve

  • Identifying new methods to diagnose, prevent and treat infections before they become life-threatening.
  • Possessing large and unique collections of the most important antibiotic resistant bacteria, the Henderson group is using this research to develop solutions to the global problem of antimicrobial resistance.
  • Using animal models, bacterial mutants identified in the high throughput screens are assessed for important for infectious disease. 

The Henderson group has successfully introduced into patients the first novel treatment for infectious diseases since the last class of antibiotics was discovered more than 30 years ago. 

Research areas

  • Immune response to bacterial infections
  • Antimicrobials
  • Protein secretion
  • Cell envelope biology
  • Bacterial pathogenesis

  • Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48-metalloprotease BepA

    Bryant, Jack A., Cadby, Ian T., Chong, Zhi-Soon, Boelter, Gabriela, Sevastsyanovich, Yanina R., Morris, Faye C., Cunningham, Adam F., Kritikos, George, Meek, Richard W., Banzhaf, Manuel, Chng, Shu-Sin, Lovering, Andrew L. and Henderson, Ian R. (2021). Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48-metalloprotease BepA. Journal of Bacteriology, 203 (2) e00434-20, e00434-20. doi: 10.1128/jb.00434-20

  • Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization

    Bryant, Jack Alfred, Morris, Faye C., Knowles, Timothy J., Maderbocus, Riyaz, Heinz, Eva, Boelter, Gabriela, Alodaini, Dema, Colyer, Adam, Wotherspoon, Peter J., Staunton, Kara A., Jeeves, Mark, Browning, Douglas F., Sevastsyanovich, Yanina R., Wells, Timothy J., Rossiter, Amanda E., Bavro, Vassiliy N., Sridhar, Pooja, Ward, Douglas G., Chong, Zhi-Soon, Goodall, Emily C. A., Icke, Christopher, Teo, Alvin, Chng, Shu-Sin, Roper, David I., Lithgow, Trevor, Cunningham, Adam F., Banzhaf, Manuel, Overduin, Michael and Henderson, Ian R. (2020). Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization. eLife, 9. doi: 10.7554/elife.62614

  • Mice deficient in T-bet form inducible NO synthase-positive granulomas that fail to constrain Salmonella

    Perez-Toledo, Marisol, Beristain-Covarrubias, Nonantzin, Channell, William M., Hitchcock, Jessica R., Cook, Charlotte N., Coughlan, Ruth E., Bobat, Saeeda, Jones, Nicholas D., Nakamura, Kyoko, Ross, Ewan A., Rossiter, Amanda E., Rooke, Jessica, Garcia-Gimenez, Alicia, Jossi, Sian, Persaud, Ruby R., Marcial-Juarez, Edith, Flores-Langarica, Adriana, Henderson, Ian R., Withers, David R., Watson, Steve P. and Cunningham, Adam F. (2020). Mice deficient in T-bet form inducible NO synthase-positive granulomas that fail to constrain Salmonella. Journal of Immunology, 205 (3), 708-719. doi: 10.4049/jimmunol.2000089

  • ASY1 acts as a dosage-dependent antagonist of telomere-led recombination and mediates crossover interference in Arabidopsis

    Lambing, Christophe, Kuo, Pallas C., Tock, Andrew J., Topp, Stephanie D. and Henderson, Ian R. (2020). ASY1 acts as a dosage-dependent antagonist of telomere-led recombination and mediates crossover interference in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America, 117 (24), 13647-13658. doi: 10.1073/pnas.1921055117

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Our team

Group Leader

Researchers

Research excellence

$1.3 billion+ commercial investment attracted to IMB research
1454 international collaborators
 
385 original publications in 2020
 
$28M in research funding last calendar year
 
20%+ of patent families at UQ are derived from IMB research
100% of donations go to the cause
 

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